Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2013 |
| Outros Autores: | , , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositório Institucional da FIOCRUZ (ARCA) |
| Texto Completo: | https://www.arca.fiocruz.br/handle/icict/33562 |
Resumo: | Universidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil. |
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Seraphim, Thiago VargasAlves, Marina De MatteuSilva, Indjara Mallmann daGomes, Francisco Edvan RodriguesSilva, Kelly Pereira daMurta, Silvane Maria FonsecaBarbosa, Leandro Ramos SouzaBorges, Júlio Cesar2019-06-18T17:35:54Z2019-06-18T17:35:54Z2013SERAPHIM, Thiago Vargas et al. Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90. PLoS One; v. 8, n. 6, p. 1-14, 2013.1932-6203https://www.arca.fiocruz.br/handle/icict/3356210.1371/journal.pone.0066822engPublic Library of ScienceHomeostase celularPlasmodium FalciparumPlasmodium FalciparumLeishmania braziliensisLow Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleUniversidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil.Universidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil / Universidade Federal de São Carlos. Centro de Ciências Biológicas e da Saúde. São Carlos, SP, Brasil.Universidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil.Universidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil.Universidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil.Fundação Oswaldo Cruz. Centro de Pesquisa René Rachou. Belo Horizonte, MG, Brasil.Universidade de São Paulo. Instituto de Física. Departamento de Física Geral. São Paulo, SP, Brasil.Universidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil.The Hsp90 molecular chaperone is essential for protein homeostasis and in the maturation of proteins involved with cell-cycle control. The low ATPase activity of Hsp90 is critical to drive its functional cycle, which is dependent on the Hsp90 cochaperones. The Activator of Hsp90 ATPase-1 (Aha1) is a protein formed by two domains, N- and C-terminal, that stimulates the Hsp90 ATPase activity by several folds. Although the relevance of Aha1 for Hsp90 functions has been proved, as well as its involvement in the desensitization to inhibitors of the Hsp90, the knowledge on its overall structure and behavior in solution is limited. In this work we present the functional and structural characterization of Leishmania braziliensis Aha1 (LbAha1). This protozoan is the causative agent of cutaneous and mucocutaneous leishmaniasis, a neglected disease. The recombinant LbAha1 behaves as an elongated monomer and is organized into two folded domains interconnected by a flexible linker. Functional experiments showed that LbAha1 interacts with L. braziliensis Hsp90 (LbHsp90) with micromolar dissociation constant in a stoichiometry of 2 LbAha1 to 1 LbHsp90 dimer and stimulates 10-fold the LbHsp90 ATPase activity showing positive cooperativity. Furthermore, the LbHsp90.info:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-83082https://www.arca.fiocruz.br/bitstream/icict/33562/1/license.txt9193a7c197bc67acd023525e72a03240MD51ORIGINALLow Resolution Structural Studies Indicate.pdfLow Resolution Structural Studies Indicate.pdfapplication/pdf1552511https://www.arca.fiocruz.br/bitstream/icict/33562/2/Low%20Resolution%20Structural%20Studies%20Indicate.pdf7035ea2e180b5d2444f02e08ba5e0f47MD52TEXTLow Resolution Structural Studies Indicate.pdf.txtLow Resolution Structural Studies Indicate.pdf.txtExtracted texttext/plain64898https://www.arca.fiocruz.br/bitstream/icict/33562/3/Low%20Resolution%20Structural%20Studies%20Indicate.pdf.txt031482a97e9c6a3347dad5448985e491MD53icict/335622019-10-14 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| dc.title.pt_BR.fl_str_mv |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 |
| title |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 |
| spellingShingle |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 Seraphim, Thiago Vargas Homeostase celular Plasmodium Falciparum Plasmodium Falciparum Leishmania braziliensis |
| title_short |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 |
| title_full |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 |
| title_fullStr |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 |
| title_full_unstemmed |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 |
| title_sort |
Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90 |
| author |
Seraphim, Thiago Vargas |
| author_facet |
Seraphim, Thiago Vargas Alves, Marina De Matteu Silva, Indjara Mallmann da Gomes, Francisco Edvan Rodrigues Silva, Kelly Pereira da Murta, Silvane Maria Fonseca Barbosa, Leandro Ramos Souza Borges, Júlio Cesar |
| author_role |
author |
| author2 |
Alves, Marina De Matteu Silva, Indjara Mallmann da Gomes, Francisco Edvan Rodrigues Silva, Kelly Pereira da Murta, Silvane Maria Fonseca Barbosa, Leandro Ramos Souza Borges, Júlio Cesar |
| author2_role |
author author author author author author author |
| dc.contributor.author.fl_str_mv |
Seraphim, Thiago Vargas Alves, Marina De Matteu Silva, Indjara Mallmann da Gomes, Francisco Edvan Rodrigues Silva, Kelly Pereira da Murta, Silvane Maria Fonseca Barbosa, Leandro Ramos Souza Borges, Júlio Cesar |
| dc.subject.other.pt_BR.fl_str_mv |
Homeostase celular Plasmodium Falciparum |
| topic |
Homeostase celular Plasmodium Falciparum Plasmodium Falciparum Leishmania braziliensis |
| dc.subject.en.pt_BR.fl_str_mv |
Plasmodium Falciparum Leishmania braziliensis |
| description |
Universidade de São Paulo. Instituto de Química de São Carlos. São Carlos, SP, Brasil. |
| publishDate |
2013 |
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2013 |
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2019-06-18T17:35:54Z |
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2019-06-18T17:35:54Z |
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info:eu-repo/semantics/article |
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SERAPHIM, Thiago Vargas et al. Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90. PLoS One; v. 8, n. 6, p. 1-14, 2013. |
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https://www.arca.fiocruz.br/handle/icict/33562 |
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1932-6203 |
| dc.identifier.doi.none.fl_str_mv |
10.1371/journal.pone.0066822 |
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SERAPHIM, Thiago Vargas et al. Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90. PLoS One; v. 8, n. 6, p. 1-14, 2013. 1932-6203 10.1371/journal.pone.0066822 |
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